Lc 8a

Manufactured by Shimadzu

Sourced in Japan

The Shimadzu LC-8A is a high-performance liquid chromatography (HPLC) system designed for various analytical applications. It features a modular design, allowing for the integration of different components, such as pumps, auto-samplers, and detectors, to create a customized analytical solution. The core function of the LC-8A is to separate, identify, and quantify components within a liquid sample.

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Lab products found in correlation

Silica gel 60, by Merck Group (3 mentions) Silica gel 60 f254, by Merck Group (3 mentions) Avance 3 600 spectrometer, by Bruker (3 mentions) Ez purify 3 system, by Merck Group (3 mentions) Prc ods k column, by Agilent Technologies (3 mentions) Spd m10 av, by Phenomenex (2 mentions) Silica gel 60 rp 18 f254s, by Merck Group (2 mentions) Precoated silica gel gf254 plates, by Qingdao Marine Chemical (2 mentions) Rp 18 silica gel, by Merck Group (2 mentions) Ft ir 480 spectrophotometer, by Jasco (2 mentions) Model 343, by PerkinElmer (2 mentions) Si gel, by Merck Group (2 mentions) Mass spectrophotometer, by JEOL (2 mentions) Drx 300 spectrophotometer, by Bruker (2 mentions) Si gf256, by Merck Group (2 mentions) Whatman, by Cytiva (2 mentions) Zorbax sb c 18 75, by Agilent Technologies (2 mentions) Spd m10 av, by Shimadzu (1 mentions) Sulfo cyanine5 nhs ester, by Lumiprobe (1 mentions) Avance 400, by Bruker (1 mentions)

Close spelling variants of this product

LC-8A system (16 citations) LC-8A pump (14 citations) LC-8A series pumping system (6 citations) LC-8a series HPLC system (3 citations) LC-8A preparative LC (3 citations) Model LC-8A (3 citations) LC-8A pump system (3 citations) LC-8A HPLC (2 citations) LC-8A HPLC system (2 citations)

40 protocols using lc 8a

Synthesis and Characterization of Systemin Peptides

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Two different peptides were produced: Sys and Sys-scramble (Scp), the latter was used as control. Peptides synthesis, purification and stability are described elsewhere [40 (link)]. Briefly, the peptides were obtained by solid phase synthesis following standard protocols [41 (link)]. Purification of the peptides was carried out by Reversed-Phase High-Performance Liquid Chromatography (RP-HPLC) (Shimadzu LC-8A, equipped with a SPD-M10 AV) on a semipreparative column (Jupiter 10µProteo 90A, 250 × 10.0 mm, Phenomenex, Torrance, CA, USA) using a gradient of acetonitrile (0.1% TFA) in water (0.1% TFA) from 5 to 50% in 30 min at 5 mL/min. Peptides were characterized by mass spectrometry (LC-MS ESI-TOF 6230 Agilent Technologies, Milan, Italy). Systemin sequence: AVQSKPPSKRDPPKMQTD. Mass calculated: 2009.3 Mass found: 670.94 [M + 3H]³⁺; 1005.60 [M + 2H]²⁺.
Systemin scramble sequence: KSKMDRQPVQAPDKPSPT. Mass calculated: 2009.3 Mass found: 670.96 [M + 3H]³⁺; 1005.53 [M + 2H]²⁺.
Peptide stability was tested as previously described [40 (link)]. Analysis of the HPLC (Shimadzu LC-8A, equipped with a SPD-M10 AV) profiles and of the mass spectra collected indicates that the peptide is stable in all the tested conditions [40 (link)]. Stock solutions of the synthesized peptides were prepared as described in [42 ].

Coppola M., Di Lelio I., Romanelli A., Gualtieri L., Molisso D., Ruocco M., Avitabile C., Natale R., Cascone P., Guerrieri E., Pennacchio F, & Rao R. (2019). Tomato Plants Treated with Systemin Peptide Show Enhanced Levels of Direct and Indirect Defense Associated with Increased Expression of Defense-Related Genes. Plants, 8(10), 395.

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Peptide Synthesis and Characterization Protocol

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All peptides were synthesized via solid phase 9-fluorenylmethoxycarbonyl (Fmoc) chemistry and procured from Genscript Co. (Piscataway, NJ), with the exception of 4Iphf-HN17 and Bombesin which were synthesized in house (Table 1). The fluorescent dye fluorescein-5,6-isothiocyanate (FITC) was conjugated to all the peptides at the N-terminus via Ahex chemistry with the exception of 4Iphf-HN17 which was dye-conjugated via the lysine. Fractions with >90% purity were pooled via preparative high-performance liquid chromatography (HPLC, Shimadzu, LC-8A) and analyzed using mass spectral analysis. Sulfo-Cyanine5 NHS ester (Lumiprobe Corporation) was substituted for FITC for lead peptide evaluation in vivo to enhance detectability. Lyophilized peptides were sequentially dissolved in DMSO and water to a final concentration of 1 mM, aliquoted, and stored at −20°C until use.

Locke L.W., Shankaran K., Gong L., Stoodley P., Vozar S.L., Cole S.L., Tweedle M.F, & Wozniak D.J. (2020). Evaluation of peptide-based probes towards in vivo diagnostic imaging of bacterial biofilm-associated infections. ACS infectious diseases, 6(8), 2086-2098.

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Purification and Characterization of Synthetic Intermediates

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All chemicals and solvents were purchased from Sigma-Aldrich or Fisher Scientific and were used as obtained without further purification. Synthetic intermediates were purified on 230–400 mesh silica gel using a Teledyne CombiFlash R_f flash chromatograph. ¹H, ¹³C, and ¹⁹F NMR spectra were recorded on Bruker DPX-400 or AVANCE-400 spectrometers at 400 MHz, 100 MHz, and 376 MHz, respectively. NMR chemical shifts are reported in δ (ppm) using residual solvent peaks as standards (CDCl₃−7.26 (H), 77.16 (C); CD₃OD−3.31 (H), 49.00 (C)). High resolution mass spectra (HRMS) were acquired using an LCMS-IT-TOF (Shimadzu) mass spectrometer in ESI mode. Preparative HPLC purification of synthetic intermediates was performed on a Shimadzu LC-8A instrument with an ACE 5AQ column (150 × 21.2 mm, particle size 5 μm; eluent: 8 – 100% MeOH (0.05% TFA)/H₂O (0.05% TFA) gradient, 30 min; flow rate: 17 mL/min; UV detection at 220 and 254 nm). The purity of all final compounds (greater than 95% in all cases) was determined by analytical HPLC on an ACE 3AQ C₁₈ column (150 × 4.6 mm, particle size 3 μm; eluent: MeOH (0.05% TFA)/H₂O (0.05% TFA) gradient, 25 min; flow rate: 1.0 mL/min).
The synthetic procedures and characterization data of all intermediates can be found in the Supporting Information.

Zhang G., McCorvy J.D., Shen S., Cheng J., Roth B.L, & Kozikowski A.P. (2019). Design of Fluorinated Cyclopropane Derivatives of 2-Phenylcyclopropylmethylamine Leading to Identification of a Selective Serotonin 2C (5-HT2C) Receptor Agonist without 5-HT2B Agonism. European journal of medicinal chemistry, 182, 111626.

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Synthesis and Purification of Peptide Compounds

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SAPs (Table 1) were commercially synthesized by Shanghai Bootech Bioscience & Technology Co., Ltd. (Shanghai, People’s Republic of China). Peptides were purified to higher than 95% by high-performance liquid chromatography (Shimadzu LC-8A; Shimadzu Corporation, Kyoto, Japan), and their molecular weights were determined by mass spectrometer (LCQ Deca XP Max; Thermo Fisher Scientific, Waltham, MA, USA). Lyophilized peptide was dissolved at a concentration of 10 mg/mL in sterile water and used as a stock solution.

Liu S., Zhang L., Cheng J., Lu Y, & Liu J. (2016). Sustained release of hepatocyte growth factor by cationic self-assembling peptide/heparin hybrid hydrogel improves β-cell survival and function through modulating inflammatory response. International Journal of Nanomedicine, 11, 4875-4890.

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Synthetic SOCS3 Mimetic Peptides

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The SOCS3 mimetic peptides, named KIR or KIR-ESS, were designed starting from structural and biochemical studies of SOCS3/Jak2 complex [18 (link)]. Control peptides (Ctrl1 and Ctrl2) were identical to SOCS3 KIR-ESS region with aminoacid substitutions in positions critical for SOCS3 and Jak2 interactions (Table 1). Peptides were synthesized through solid phase peptide synthesis, performed on a fully automated multichannel peptide synthesizer Syro I (Multisynthech, Witten, Germany). Preparative RP-HPLC was carried out on a Shimadzu LC-8A, equipped with a SPD-M10 AV detector and a Phenomenex C18 Jupiter column (50 × 22 mm ID; 10 μm) (Shimadzu, Japan). Peptides were then, analyzed by mass spectrometry, carried out on an LCQ DECA XP Ion Trap mass spectrometer equipped with an OPTON ESI source, operating at 4.2 kV and 320°C, and with a complete Surveyor HPLC system (ThermoFisher Scientific, Waltham, MA USA). To facilitate the peptide delivery into cell cytoplasm, the fragment 48–60 of the HIV Tat protein was conjugated to SOCS3 or to control peptides in a stepwise manner. Purified peptides were lyophilized and stored at −20°C until use.

Madonna S., Scarponi C., Morelli M., Sestito R., Scognamiglio P.L., Marasco D, & Albanesi C. (2017). SOCS3 inhibits the pathological effects of IL-22 in non-melanoma skin tumor-derived keratinocytes. Oncotarget, 8(15), 24652-24667.

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Analytical and Preparative RP-HPLC Peptide Purification

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Analytical RP-HPLC was carried out using a C18 column (Phenomenex, Luna 5u, 4.6mm X 250mm). The peptide samples were eluted from the column by employing a linear gradient of solvent B (5–90% B in 130 min; solvent B, 80% acetonitrile in water containing 0.1% aqueous TFA; solvent A, 0.1% TFA; flow rate: 1 ml/min). Preparative RP-HPLC (LC-8A Shimadzu Preparative Liquid Chromatograph) was used for large-scale purification of peptides using a preparative column (Phenomenex preparatory C18 column, Luna 10 μ, 30 mm X 250 mm). The chromatography was carried out using the same solvent gradient system as above but at a flow rate of 30 ml/min.

Singh S., Gupta K., Shukla S., Sampathkumar S.G, & Roy R.P. (2019). Sortase-click strategy for defined protein conjugation on a heptavalent cyclodextrin scaffold. PLoS ONE, 14(5), e0217369.

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Prodigiosin Quantification by HPLC

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The purified prodigiosin was dissolved in methanol and syringe filtered (0.2 µm) immediately before HPLC analysis. Chromatographic separation was carried out using an RP-18 column for isocratic chromatography (Shimadzu LC-8A, 5 µm, 18 × 100 mm), with a flow rate of 1 ml min^-1 and an injection volume of 10 µL. The solvents used were methanol/10 mM triethylamine (19/1, v/v). The wavelength for detection was 533 nm. The concentration of prodigiosin was identified by measuring the absorbance, and then calculated using a standard correlation curve between absorbance and the dry weight of prodigiosin.

Darshan N, & Manonmani H.K. (2016). Prodigiosin inhibits motility and activates bacterial cell death revealing molecular biomarkers of programmed cell death. AMB Express, 6, 50.

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Retinal Retinoic Acid Quantification

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The retinal retinoic acid level at weeks 2 and 4 was detected after corresponding biometric measurements were completed. The level of RA in the retina was detected using high performance liquid chromatography (HPLC, LC-8A, SHIMADZU.co, Japan) with an electrochemical detector (Couloehem111, ESA, USA). After the guinea pigs were sacrificed by cervical dislocation, eyes were removed and hemisected on the line of the ora serrata. The retinal layer was carefully dissected from the RPE, and all pigmented cells were removed to ensure RPE was not collected. Procedures were carried out on ice and under dim red light. The atRA standard sample was purchased from Sigma (C₂₀H₂₈O₂; molecular mass, 300.44). Concentration of retinal RA (µg) in each tissue was determined using methods reported in previous studies.²⁷ (link)

Yu M., Liu W., Wang B, & Dai J. (2021). Short Wavelength (Blue) Light Is Protective for Lens-Induced Myopia in Guinea Pigs Potentially Through a Retinoic Acid–Related Mechanism. Investigative Ophthalmology & Visual Science, 62(1), 21.

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Bioactive Compounds Extraction from Schisandra chinensis

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The Schisandra chinensis was purchased from TCM market in Seoul, Korea in September 2017. Voucher specimens (GL0680) were authenticated by us and were deposited by Dr. Chun Whan Choi at the herbarium of Bio-center, Gyeonggi Institute of Science & Technology Promotion, Suwon, South Korea. ¹H and ¹³C NMR experiments were performed on a Bruker Ascend 700 MHz spectrometer with tetramethylsilane (TMS). LC-ESI-MS were obtained on a Triple TOF 5600+ instrument (AB SCIEX, MA, USA) and HRESI-MS on a LTQ Orbitrap XL instrument (Thermo Scientific, MA, USA). Thin Layer Chromatography (TLC) was conducted on Silica gel 60 F₂₅₄ (Merck, Darmstadt, Germany) and Silica gel 60 RP-18 F_254S (Merck, Darmstadt, Germany) plates. Column chromatography (CC) was performed using Silica gel 60 (70~230 mesh, Merck, Germany), ODS-A (12 nm S-7 μm, YMC GEL, Tokyo, Japan), and preparative high performance liquid chromatography (HPLC) was performed on LC-8A (Shimadzu, Japan).

Jang Y., Lee J.H., Lee M.J., Kim S.J., Ju X., Cui J., Zhu J., Lee Y.L., Namgung E., Sung H.W., Lee H.W., Ryu M.J., Oh E., Chung W., Kweon G.R., Choi C.W, & Heo J.Y. (2020). Schisandra Extract and Ascorbic Acid Synergistically Enhance Cognition in Mice through Modulation of Mitochondrial Respiration. Nutrients, 12(4), 897.

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Isolation and Characterization of Persicaria senticosa

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Persicaria senticosa was collected from Seo-myeon, Chuncheon-si, Gangwon-do, Korea, in 2016 (GPS: N 37° 55′ 30.1^″, E 127° 37′ 57.0^″, altitude: 434 m). Voucher specimens (G071) were authenticated by Dr. Chun Whan Choi. Persicaria senticosa were deposited at the herbarium of Biocenter, Gyeonggido Business & Science Accelerator, Suwon, South Korea (Fig. S3). The 99.9% methanol extract of thirty-four Polygonum was obtained from the Korea Plant Extract Bank at the Korea Research Institute of Bioscience and Biotechnology (Daejeon, Korea). ¹H and ¹³C NMR experiments were performed on a Bruker Ascend 700 MHz spectrometer with tetramethylsilane (TMS). LC-ESI-MS was obtained on a Triple TOF 5600+ instrument (AB SCIX, USA) and HRESI-MS on a LTQ Orbitrap XL instrument (Thermo, USA). Thin-layer chromatography (TLC) was conducted on Silica gel 60 F₂₅₄ (Merck, Germany) and Silica gel 60 RP-18 F_254S (Merck, Germany) plates. Column chromatography(CC) was performed using Silica gel 60 (70~230 mesh, Merck, Germany), ODS-A (12 nm S-7 μm, YMC GEL, Japan), and preparative HPLC was performed on LC-8A (Shimadzu, Japan).

Choi Y.H., Lee J.Y., Lee J.E., Jung Y.W., Jeong W., Hong S.S., Cho Y.R, & Choi C.W. (2020). Skin-Related Properties and Constituents from the Aerial Parts Extract of Persicaria senticosa. Oxidative Medicine and Cellular Longevity, 2020, 6627752.

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